1AZR

CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA ZINC AZURIN MUTANT ASP47ASP AT 2.4 ANGSTROMS RESOLUTION

Summary for 1AZR

• Entry DOI: 10.2210/pdb1azr/pdb
• Descriptor: AZURIN, COPPER (II) ION, NITRATE ION, ... (4 entities in total)
• Functional Keywords: electron transfer(cuproprotein)
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 4
• Total formula weight: 56163.39

Authors

Sjolin, L.,Tsai, Lc.,Langer, V.,Pascher, T.,Karlsson, G.,Nordling, M.,Nar, H. (deposition date: 1993-03-04, release date: 1993-07-15, Last modification date: 2024-11-20)

Primary citation

Sjolin, L.,Tsai, L.C.,Langer, V.,Pascher, T.,Karlsson, G.,Nordling, M.,Nar, H.
Structure of Pseudomonas aeruginosai zinc azurin mutant Asn47Asp at 2.4 A resolution.
Acta Crystallogr.,Sect.D, 49:449-457, 1993

PubMed Abstract: The Pseudomonas aeruginosa azurin mutant Asn47Asp has been isolated, its spectroscopic and kinetic properties characterized, and the X-ray crystal structure of its zinc derivative determined. While the optical and electron paramagnetic resonance spectra as well as the electron-transfer activity of the mutant are very similar to the wild-type values, the Asn47Asp reduction potential is slightly increased by 20 mV. The mutant crystallized in the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 57.8, b = 81.5 and c = 112.6 A. There are four molecules in the asymmetric unit, packed as a tetramer which consists of two independent dimers. The zinc site of this mutant structure is similar to the wild-type zinc azurin and, in particular, the metal-binding site is almost identical to the site found in the wild-type zinc-azurin structure [Nar, Huber, Messerschmidt, Filippou, Barth, Jaquinod, Kamp & Canters (1992). Eur. J. Biochem. 205, 1123-1129]. The Asp47 side chain at that mutation site takes on a very similar orientation to Asn47 in the wild-type structure preserving the two hydrogen bonds with the neighbouring Thr113 NH and O(gamma)H. Therefore, the increased reduction potential of the mutant is probably a result of an altered charge distribution close to the metal site.

PubMed: 15299504
DOI: 10.1107/S0907444993005207

Experimental method

X-RAY DIFFRACTION (2.4 Å)